The N-Terminal Region of the Escherichia coli WecA (Rfe) Protein, Containing Three Predicted Transmembrane Helices, Is Required for Function but Not for Membrane Insertion
AUTOR(ES)
Amer, Amal O.
FONTE
American Society for Microbiology
RESUMO
The correct site for translation initiation for Escherichia coli WecA (Rfe), presumably involved in catalyzing the transfer of N-acetylglucosamine 1-phosphate to undecaprenylphosphate, was determined by using its FLAG-tagged derivatives. The N-terminal region containing three predicted transmembrane helices was found to be necessary for function but not for membrane localization of this protein.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=94301Documentos Relacionados
- The N-terminal 22 amino acid residues in the lactose permease of Escherichia coli are not obligatory for membrane insertion or transport activity.
- Identification of an N-Terminal Region of Sigma 54 Required for Enhancer Responsiveness
- The N-terminal region of DNA polymerase δ catalytic subunit is necessary for holoenzyme function
- Transmembrane orientation of signal-anchor proteins is affected by the folding state but not the size of the N-terminal domain.
- Mutations in the N-Terminal Region of Influenza Virus PB2 Protein Affect Virus RNA Replication but Not Transcription